ID A5KC62_PLAVS Unreviewed; 981 AA.
AC A5KC62;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=PVX_096270 {ECO:0000313|EMBL:EDL43080.1};
OS Plasmodium vivax (strain Salvador I).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=126793 {ECO:0000313|EMBL:EDL43080.1, ECO:0000313|Proteomes:UP000008333};
RN [1] {ECO:0000313|EMBL:EDL43080.1, ECO:0000313|Proteomes:UP000008333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Salvador I {ECO:0000313|EMBL:EDL43080.1,
RC ECO:0000313|Proteomes:UP000008333};
RX PubMed=18843361; DOI=10.1038/nature07327;
RA Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., Caler E.,
RA Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., Cheng Q., Coulson R.M.,
RA Crabb B.S., Del Portillo H.A., Essien K., Feldblyum T.V.,
RA Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., Kang'a S.,
RA Kooij T.W., Korsinczky M., Meyer E.V., Nene V., Paulsen I., White O.,
RA Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., Stoeckert C.J.,
RA Sullivan S.A., Yamamoto M.M., Hoffman S.L., Wortman J.R., Gardner M.J.,
RA Galinski M.R., Barnwell J.W., Fraser-Liggett C.M.;
RT "Comparative genomics of the neglected human malaria parasite Plasmodium
RT vivax.";
RL Nature 455:757-763(2008).
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|RuleBase:RU365068};
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000256|RuleBase:RU365068}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDL43080.1}.
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DR EMBL; AAKM01000020; EDL43080.1; -; Genomic_DNA.
DR RefSeq; XP_001612807.1; XM_001612757.1.
DR AlphaFoldDB; A5KC62; -.
DR STRING; 126793.A5KC62; -.
DR EnsemblProtists; EDL43080; EDL43080; PVX_096270.
DR GeneID; 5472054; -.
DR KEGG; pvx:PVX_096270; -.
DR InParanoid; A5KC62; -.
DR OMA; VFLSNCH; -.
DR Proteomes; UP000008333; Chromosome 3.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR PANTHER; PTHR24031:SF89; ATP-DEPENDENT RNA HELICASE DDX31-RELATED; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365068};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU365068};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365068};
KW Reference proteome {ECO:0000313|Proteomes:UP000008333};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 151..329
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 460..668
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 981 AA; 109694 MW; 29C17F24F232B6A6 CRC64;
MGKFRGGKDK KQPGKGGIKK SPKKGIQKGI KKGGKIVPKI VPKGGEIPPP KKQANKQAKK
QAKKQAKKQA TRPAKPLTNT PTEETYLQSS GSSVGGAPLD APSPEVPCGS PGGGLFDGLF
ADLKGVLSES LLQTLEKNNF VQTTSIQKRS IPIVLRDNDV FLKSMTGSGK TLSYALPSIQ
KILNLQKEKI KITRDMGTFI LVLSPTRELA IQINSLFTTL TKPYPYIVVS CLTGGEKKKS
EKNRLKKGVS ILTCTPGRLL DHLEHTKGLK LSFLQSLILD EADKVIFLGS QDRVRLIFDA
NFQMVFISAT LNHAVKSLAN YCLTNRTVWV EAKEDGAPGG GLSGELSGEL SGGVVVQPST
HEEEVTPTVG EDDWKYDLPE QLKQFCIVTD FRKKFLCLVH LLLSCMKKKQ KPVVFLSNCH
SVEYMGALLK SLYWPTDLKK ENMEVHKKLH KGIPSVLLKE DEQLLRKHLE QTLQRRECQL
AGDPSKRRKK GGITLPFKNI HVDDLLGEDS CDERNGSAGG GDRSALYNVS TDRHKRKYLF
GDTHIYTLHG NMSKEDRLGN FLDFANGKRG DNCILLCTEI VSRGVNLDEL SVVVQYDPPQ
VFEEYVHKVG RTARLQKEGT SYLFLLPTEV EFLNVLREKK IHVKTIRGEE LIGKFRREDV
PPSFASIGGD LLSFIYNHFK VTVKSDESLM EKATSAFLAS VTAYYSVSKP LRHIFCAKSL
HLGHLAYAFL LDESPREIAQ LNKQQRYLRV KRHTTLGKRE RRLLRGGASA AQLDAVKKYL
KSFDHKNEEE SINGFAQLLK QLNIKMAVFD FDLTIIGAHS GGYIDKANDV GHIGTAVTNH
FKLLSKALKE NGIKITVATF SDEEAIRYSR GRNPTLIAGT DMVKFSMQQS KCDAKIEKVY
AYYPPYYREP RHYRQLGMDK PMSHDKSYHL KQIRTDFGVN VDEILFVDDD VNNCTSAKKE
GYLTFNVTGK NGFNFKSVKV M
//
